Information on EC 1.10.3.12 - menaquinol oxidase (H+-transporting)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.10.3.12
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RECOMMENDED NAME
GeneOntology No.
menaquinol oxidase (H+-transporting)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 menaquinol + O2 = 2 menaquinone + 2 H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
menaquinol:O2 oxidoreductase (H+-transporting)
Cytochrome aa3-600, one of the principal respiratory oxidases from Bacillus subtilis, is a member of the heme-copper superfamily of oxygen reductases, and is a close homologue of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, but uses menaquinol instead of ubiquinol as a substrate.The enzyme also pumps protons across the membrane bilayer, generating a proton motive force.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the FMN enzyme protoporphyrinogen IX oxidase (HemG) of Escherichia coli abstracts six electrons from its substrate and transfers them via ubiquinone, cytochrome bo3 and cytochrome bd oxidase to oxygen. Under anaerobic conditions electrons are transferred via menaquinone, fumarate and nitrate reductase. Cyo, Cyd and Nar contribute to the proton motive force that drives ATP formation. oxygen-dependent cytochrome oxidases, cytochrome bo3 (Cyo) and cytochrome bd (Cyd) oxidase, sustain up to 67% (Cyd) and 78% (Cyo) of HemG activity in the absence of ubiquinone, indicating a tight association of the quinones with the enzyme complexes during preparation
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dimethyl-1,4-naphthoquinol + O2
2,3-dimethyl-1,4-naphthoquinone + H2O
show the reaction diagram
2,3-dimethyl-1,4-naphthoquinone + O2
2,3-dimethyl-1,4-naphthoquinol + H2O
show the reaction diagram
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?
duroquinol + O2
duroquinone + H2O
show the reaction diagram
ferricytochrome c + O2
ferrocytochrome c + H2O
show the reaction diagram
menadiol + O2
menadione + H2O
show the reaction diagram
menaquinol + O2
menaquinone + H2O
show the reaction diagram
NADH + O2
?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
menaquinol + O2
menaquinone + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(n-heptyl)-4-hydroxyquinoline-N-oxide
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antimycin A
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more than 10fold less effective than 2-(n-heptyl)-4-hydroxyquinoline-N-oxide, 39% residual activity at 0.01 mM
cyanide
Myxothiazol
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more than 10fold less effective than 2-(n-heptyl)-4-hydroxyquinoline-N-oxide, 45% residual activity at 0.01 mM
Stigmatellin
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more than 10fold less effective than 2-(n-heptyl)-4-hydroxyquinoline-N-oxide, 39% residual activity at 0.01 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
2,3-dimethyl-1,4-naphthoquinone
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in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
61 - 65
2,3-dimethyl-1,4-naphthoquinone
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13686
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
15000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
20000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
22670
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
33640
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
54000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
57000
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the preparation consists of two major (57000 Da and 36000 Da) polypeptides
73834
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
144000
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calculated from sequence of cDNA
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and chromatofocusing
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Ni-NTA column chromatography, 1.25 equivalents of menaquinone-7 co-purify with the enzyme
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Ni2+-chelating-Sepharose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Bacillus subtilis strain LUW143 lacking both the aa3-600 menaquinol oxidase and caa3-type cytochrome c oxidase
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expressed in Bacillus subtilis strain LUW20
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